Thiostrepton binds to malarial plastid rRNA

Barbara Clough; Malcolm Strath; Peter Preiser; Paul Denny; Wilson

doi:10.1016/S0014-5793(97)00241-X

Thiostrepton binds to malarial plastid rRNA

Barbara Clough^*, Malcolm Strath, Peter Preiser, Paul Denny, Wilson

^*Corresponding author for this work

Medical Research Council

Research output: Contribution to journal › Article › peer-review

87 Citations (Scopus)

Abstract

Binding of the thiazolyl peptide antibiotic thiostrepton to the GTPase domain of 23S rRNA involves a few crucial nucleotides, notably A1067 (E. coli). Small RNA transcripts were prepared corresponding to the GTPase domain of the plastid 23S rRNA and the two forms of cytosolic 28S rRNAs found in the human malaria parasite Plasmodium falciparum, as well as the plastid form of rRNA of the AIDS-related pathogen Toxoplasma gondii. Binding affinities of the wild type and mutated RNA sequences were as predicted; the malarial plastid sequence had by far the highest affinity, whereas that from toxoplasma did not bind thiostrepton.

Original language	English
Pages (from-to)	123-125
Number of pages	3
Journal	FEBS Letters
Volume	406
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(97)00241-X
Publication status	Published - Apr 7 1997
Externally published	Yes

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

GTPase domain
Malaria
rRNA
Thiostrepton
Toxoplasma

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0014-5793(97)00241-X

Cite this

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title = "Thiostrepton binds to malarial plastid rRNA",

abstract = "Binding of the thiazolyl peptide antibiotic thiostrepton to the GTPase domain of 23S rRNA involves a few crucial nucleotides, notably A1067 (E. coli). Small RNA transcripts were prepared corresponding to the GTPase domain of the plastid 23S rRNA and the two forms of cytosolic 28S rRNAs found in the human malaria parasite Plasmodium falciparum, as well as the plastid form of rRNA of the AIDS-related pathogen Toxoplasma gondii. Binding affinities of the wild type and mutated RNA sequences were as predicted; the malarial plastid sequence had by far the highest affinity, whereas that from toxoplasma did not bind thiostrepton.",

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doi = "10.1016/S0014-5793(97)00241-X",

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T1 - Thiostrepton binds to malarial plastid rRNA

AU - Clough, Barbara

AU - Strath, Malcolm

AU - Preiser, Peter

AU - Denny, Paul

AU - Wilson,

PY - 1997/4/7

Y1 - 1997/4/7

N2 - Binding of the thiazolyl peptide antibiotic thiostrepton to the GTPase domain of 23S rRNA involves a few crucial nucleotides, notably A1067 (E. coli). Small RNA transcripts were prepared corresponding to the GTPase domain of the plastid 23S rRNA and the two forms of cytosolic 28S rRNAs found in the human malaria parasite Plasmodium falciparum, as well as the plastid form of rRNA of the AIDS-related pathogen Toxoplasma gondii. Binding affinities of the wild type and mutated RNA sequences were as predicted; the malarial plastid sequence had by far the highest affinity, whereas that from toxoplasma did not bind thiostrepton.

AB - Binding of the thiazolyl peptide antibiotic thiostrepton to the GTPase domain of 23S rRNA involves a few crucial nucleotides, notably A1067 (E. coli). Small RNA transcripts were prepared corresponding to the GTPase domain of the plastid 23S rRNA and the two forms of cytosolic 28S rRNAs found in the human malaria parasite Plasmodium falciparum, as well as the plastid form of rRNA of the AIDS-related pathogen Toxoplasma gondii. Binding affinities of the wild type and mutated RNA sequences were as predicted; the malarial plastid sequence had by far the highest affinity, whereas that from toxoplasma did not bind thiostrepton.

KW - GTPase domain

KW - Malaria

KW - rRNA

KW - Thiostrepton

KW - Toxoplasma

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DO - 10.1016/S0014-5793(97)00241-X

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JO - FEBS Letters

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ER -

Thiostrepton binds to malarial plastid rRNA

Abstract

ASJC Scopus Subject Areas

Keywords

UN SDGs

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